Identification of the polypyrimidine tract binding protein-associated splicing factor·p54(nrb) complex as a candidate DNA double-strand break rejoining factor

Catherine L. Bladen, Durga Udayakumar, Yoshihiko Takeda, William S. Dynan

Research output: Contribution to journalArticle

75 Citations (Scopus)

Abstract

The biological effects of ionizing radiation are attributable, in large part, to induction of DNA double-strand breaks. We report here the identification of a new protein factor that reconstitutes efficient double-strand break rejoining when it is added to a reaction containing the five other polypeptides known to participate in the human nonhomologous end-joining pathway. The factor is a stable heteromeric complex of polypyrimidine tract-binding protein-associated splicing factor (PSF) and a 54-kDa nuclear RNA-binding protein (p54(nrb)). These polypeptides, to which a variety of functions have previously been attributed, share extensive homology, including tandem RNA recognition motif domains. The PSF·p54(nrb) complex cooperates with Ku protein to form a functional preligation complex with substrate DNA. Based on structural comparison with related proteins, we propose a model where the four RNA recognition motif domains in the heteromeric PSF·p54(nrb) complex cooperate to align separate DNA molecules.

Original languageEnglish (US)
Pages (from-to)5205-5210
Number of pages6
JournalJournal of Biological Chemistry
Volume280
Issue number7
DOIs
StatePublished - Feb 18 2005

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Polypyrimidine Tract-Binding Protein
Protein Splicing
Double-Stranded DNA Breaks
Nuclear RNA
Peptides
RNA-Binding Proteins
DNA
Nuclear Proteins
Ionizing Radiation
RNA
Proteins
Ionizing radiation
Joining
Molecules
Substrates
RNA Recognition Motif

ASJC Scopus subject areas

  • Biochemistry

Cite this

Identification of the polypyrimidine tract binding protein-associated splicing factor·p54(nrb) complex as a candidate DNA double-strand break rejoining factor. / Bladen, Catherine L.; Udayakumar, Durga; Takeda, Yoshihiko; Dynan, William S.

In: Journal of Biological Chemistry, Vol. 280, No. 7, 18.02.2005, p. 5205-5210.

Research output: Contribution to journalArticle

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AB - The biological effects of ionizing radiation are attributable, in large part, to induction of DNA double-strand breaks. We report here the identification of a new protein factor that reconstitutes efficient double-strand break rejoining when it is added to a reaction containing the five other polypeptides known to participate in the human nonhomologous end-joining pathway. The factor is a stable heteromeric complex of polypyrimidine tract-binding protein-associated splicing factor (PSF) and a 54-kDa nuclear RNA-binding protein (p54(nrb)). These polypeptides, to which a variety of functions have previously been attributed, share extensive homology, including tandem RNA recognition motif domains. The PSF·p54(nrb) complex cooperates with Ku protein to form a functional preligation complex with substrate DNA. Based on structural comparison with related proteins, we propose a model where the four RNA recognition motif domains in the heteromeric PSF·p54(nrb) complex cooperate to align separate DNA molecules.

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